2bjo
Crystal Structure of the Organic Hydroperoxide Resistance Protein OhrB of Bacillus subtilisCrystal Structure of the Organic Hydroperoxide Resistance Protein OhrB of Bacillus subtilis
Structural highlights
FunctionOHRB_BACSU Involved in organic hydroperoxide resistance.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the fully oxidized form of the Bacillus subtilis organic hydroperoxide-resistance (OhrB) protein is reported at 2.1 A resolution. The electron density reveals an intact catalytic disulfide bond (Cys55-Cys119) in each of the two molecules, which are intertwined into a canonical obligate dimer. However, the stereochemistry of the disulfides is unorthodox and strained, suggesting that they are sensitive to reducing agents. A deep solvent-accessible gorge reaching Cys55 may represent the access route for the reductant. Structure of the Bacillus subtilis OhrB hydroperoxide-resistance protein in a fully oxidized state.,Cooper DR, Surendranath Y, Devedjiev Y, Bielnicki J, Derewenda ZS Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1269-73. Epub 2007, Nov 16. PMID:18084074[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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